P0CP66 · CPK1_CRYNJ
- ProteinMitogen-activated protein kinase CPK1
- GeneCPK1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids366 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Responds to activation by environmental stress by phosphorylating downstream targets.
Catalytic activity
- L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
Cofactor
Activity regulation
Activated by tyrosine and threonine phosphorylation.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | MAP kinase activity | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | intracellular signal transduction | |
Biological Process | protein phosphorylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMitogen-activated protein kinase CPK1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Tremellomycetes > Tremellales > Cryptococcaceae > Cryptococcus > Cryptococcus neoformans species complex
Accessions
- Primary accessionP0CP66
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000186324 | 1-366 | Mitogen-activated protein kinase CPK1 | |||
Sequence: MTIDQSQINFNVPSTYKLEEIVGEGAYGLVVAGTHLPSGTQVAIKRITPFDHTMFCQRTLREIKLLRHFHHENIISILDLIQPESYEVFNEVYLVQELMETDLHRVIRSQELSDDHCQYFVYQTLRGLKALHSADVLHRDLKPSNLLLNANCDLKICDFGLARSSAKPPPGTSDGGQGFMTEYVATRWYRAPEVMLSFQEYTKAIDLWSVGCILAEMINGKPLFPGRDYHHQLSLILQVLGTPTMDDFNEITSQRSKDYLRALEFTRRQDFSAICPKAKPAAVDLLKQTLTFSPSKRITVEEALMHSYVEAYHDPHDEPNAEPLKPGFFDFEFHQEKLSRDQWKRMIYDEVQDPVPTILSQWTESH | ||||||
Modified residue | 181 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 183 | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
Dually phosphorylated on Thr-181 and Tyr-183, which activates the enzyme.
Keywords
- PTM
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 17-302 | Protein kinase | ||||
Sequence: KLEEIVGEGAYGLVVAGTHLPSGTQVAIKRITPFDHTMFCQRTLREIKLLRHFHHENIISILDLIQPESYEVFNEVYLVQELMETDLHRVIRSQELSDDHCQYFVYQTLRGLKALHSADVLHRDLKPSNLLLNANCDLKICDFGLARSSAKPPPGTSDGGQGFMTEYVATRWYRAPEVMLSFQEYTKAIDLWSVGCILAEMINGKPLFPGRDYHHQLSLILQVLGTPTMDDFNEITSQRSKDYLRALEFTRRQDFSAICPKAKPAAVDLLKQTLTFSPSKRITVEE | ||||||
Motif | 181-183 | TXY | ||||
Sequence: TEY |
Domain
The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
Sequence similarities
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length366
- Mass (Da)42,120
- Last updated2011-06-28 v1
- Checksum1BA353D5D67CF84E
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF414186 EMBL· GenBank· DDBJ | AAN03694.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE017345 EMBL· GenBank· DDBJ | AAW43453.1 EMBL· GenBank· DDBJ | Genomic DNA |